From Proteopedia
proteopedia linkproteopedia linkPlease do not edit this page. Eric Martz, February 2011.
Homology Model for 83-341
- Homology model of 83-341 on template chain A of 3e4c, 52% sequence identity (). Confidence in this model is high because of the 52% sequence identity and sequence alignment with only one 10-residue gap.
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Carboxy Terminus |
- .
- The seems unremarkable. Bear in mind that sidechain rotamer positions are incorrect in a homology model.
Anionic (-) / Cationic (+)
- The inner face of 95-140 is . Bear in mind that sidechain rotamer positions are incorrect in a homology model. . The distribution of hydrophobic residues in 83-140 of the homology model is similar to that in the .
- The inner face of 95-140 is , even based upon a multiple sequence alignment that includes mostly types other than 12[1] .
- When the multiple sequence alignment is limited to the 14 type-12 sequences available from Uniprot (APD 0.30), most of the residues have insufficient data, but a , namely Asn130, Val135, Val136, Glu139, Asn140. .
Homology Model for 2-88
- Swiss-Model produced a using chain A of 1dgn as template. Confidence in this model is low because the sequence alignment had only 19% identity.
- This model shows a , with a large region containing only negative charges.
Anionic (-) / Cationic (+)
- Analysis of evolutionary conservation for 2-88 is difficult because not enough related sequences are available in Uniprot. Thus most of the residues have "insufficient data" (yellow). Despite the paucity of information, there appears to be a that may be of interest. (To identify the conserved residues, toggle spinning off, then touch each residue with the mouse, and observe the popup "hover" report.)
- Cartoon
- Cartoon decorated with conserved residues
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- This model can be downloaded from model-2-88.
Notes
- ↑ ConSurf run using 80 sequences from the Uniref-90 sequence database. MSA average pairwise distance (APD) 0.94.
